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Q65LD5 (Q65LD5_BACLD) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-oxoacyl-[acyl-carrier-protein] synthase 3 2 HAMAP MF_01815
EC=2.3.1.180 HAMAP MF_01815
Alternative name(s):
3-oxoacyl-[acyl-carrier-protein] synthase III 2 HAMAP MF_01815
Beta-ketoacyl-ACP synthase III 2 HAMAP MF_01815
Gene names
Name:fabHA EMBL AAU40129.1
Synonyms:fabH2 HAMAP MF_01815
Ordered Locus Names:BL03313, BLi01221
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids By similarity. HAMAP MF_01815

Catalytic activity

Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO2. HAMAP MF_01815

Pathway

Lipid metabolism; fatty acid biosynthesis. SAAS SAAS013747 HAMAP MF_01815

Subunit structure

Homodimer By similarity. SAAS SAAS013747 HAMAP MF_01815

Subcellular location

Cytoplasm By similarity SAAS SAAS013747 HAMAP MF_01815.

Domain

The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH By similarity. HAMAP MF_01815

Sequence similarities

Belongs to the FabH family. HAMAP MF_01815

Sequences

Sequence LengthMass (Da)Tools
Q65LD5 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 59E169B1E5E51DE8

FASTA31233,877
        10         20         30         40         50         60 
MKAGIIGIGR YIPEKVLTNF DLEKMVETSD EWIRTRTGIE ERRIAAEDEK TSDMAVAAAR 

        70         80         90        100        110        120 
RAMEDANIEP EDLDMILVAT VTPDQAFPTV SCMIQEKLGA FNACAMDISA ACAGFMYGLV 

       130        140        150        160        170        180 
TGKQFIEAGT YKHVLVIGVE KLSGITDWDD RNTAVLFGDG AGAAVVGPVS DDKGILSFEL 

       190        200        210        220        230        240 
GADGRGGKHL YLDEKDHTIM NGREVFKFAV RQMGESSVNV IEKAGLSKED VDFLVPHQAN 

       250        260        270        280        290        300 
IRIMEAARER LELPVEKMSK TVHKYGNTSA ASIPISLVEE LEAGKIKDGD VIVMVGFGGG 

       310 
LTWGAIAMRW GR

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580 [Goettingen].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580 [Novozymes].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000002 Genomic DNA. Translation: AAU22783.1.
AE017333 Genomic DNA. Translation: AAU40129.1.
RefSeqYP_078421.1. NC_006270.3.
YP_090822.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65LD5.
SMRQ65LD5. Positions 1-311.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65LD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000057147; EBBACP00000055678; EBBACG00000057138.
EBBACT00000060663; EBBACP00000059096; EBBACG00000060654.
GeneID3030220.
3099878.
GenomeReviewsGene locus BLi01221 in contig AE017333_GR.
Gene locus BL03313 in contig CP000002_GR.
KEGGbld:BLi01221.
bli:BL03313.
NMPDRfig|279010.5.peg.2390.
PATRIC18948011. VBIBacLic203714_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0332.
GeneTreeEBGT00050000001269.
HOGENOMHBG649927.
OMAKEIGAIN.
PhylomeDBQ65LD5.
ProtClustDBPRK09352.

Family and domain databases

HAMAPMF_01815. FabH.
[Tree]
InterProIPR013751. ACP_syn_III.
IPR013747. ACP_syn_III_C.
IPR004655. FabH_synth.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK00648.
PfamPF08545. ACP_syn_III. 1 hit.
PF08541. ACP_syn_III_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
TIGRFAMsTIGR00747. FabH. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ65LD5_BACLD
AccessionPrimary (citable) accession number: Q65LD5
Secondary accession number(s): Q62WS5
Entry history
Integrated into UniProtKB/TrEMBL: October 25, 2004
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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